EC 2.1.1.77
Protein-beta-aspartate methyltransferase 2
PIMT 2
Protein L-isoaspartyl methyltransferase 2
L-isoaspartyl protein carboxyl methyltransferase 2

Gene name

	Name:	pcm2
	Synonyms:	pcm-2
	OrderedLocusNames:	MA_0543

From

Methanosarcina acetivorans

[TaxID: 2214]

[HAMAP proteome]

Taxonomy

Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
DOI=10.1101/gr.223902; PubMed=11932238 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.;
"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.";
Genome Res. 12:532-542(2002).

Comments

FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE010299; AAM03987.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_615507.1; -.

3D structure databases

HSSP

Q8TZR3; 1JG1. [HSSP ENTRY / PDB]

ModBase

Q8TT94.

Enzyme and pathway databases

BioCyc

MACE188937:MA0543-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004719;	Molecular function: protein-L-isoaspartate (D-aspartate) O-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from HAMAP).
GO:0030091;	Biological process: protein repair (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00090; -; 1.
PBIL [Tree]

InterPro

IPR000682; PCMT.
Graphical view of domain structure.

PANTHER

PTHR11579; PCMT; 1.

Pfam

PF01135; PCMT; 1.
Pfam graphical view of domain structure.

TIGR00080; pimt; 1.

PS01279; PCMT; 1.

Genome annotation databases

GeneID

1472435; -.

GenomeReviews

AE010299_GR; MA_0543.

KEGG

mac:MA0543; -.

NMPDR

fig|188937.1.peg.533; -.

Phylogenomic databases

HOGENOM

Q8TT94; -.

Genome annotation databases

CMR

Q8TT94; MA_0543.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 238`	`238`	`Protein-L-isoaspartate O-methyltransferase 2.`	`PRO_0000111915`
`ACT_SITE`	`82 82`		`By similarity.`

Sequence information

Length: 238 AA [This is the length of the unprocessed precursor]

Molecular weight: 26970 Da [This is the MW of the unprocessed precursor]

CRC64: 9B7EF47C884E035F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLVNAISEK DYIKDSRRRK KEEKEFEKLR KLLVEGLEDI VRDKKVLKAM FRVPRHRFVP 

        70         80         90        100        110        120 
EYEQRAAYTD RPLEIGHGQT ISTPHTVALM CEILELSEGH KVLEIGTGSG YNAAVMAELV 

       130        140        150        160        170        180 
GKTGHIYSVE RIEPLVNFAR KNLEQMGYDN VTVLLENGSM GYPRYAPYDR IAVTCAAPTI 

       190        200        210        220        230 
PKALLEQLKP GGIMVIPVGD YSQELIRVKK DSNGNIYKKR KGEVIFVPML GRHGFPRS

Q8TT94 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools